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1. Full Text Phosphorylation of the α-subunit of the eukaryotic initiation factor-2 (eIF2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
by Jiang, Hao-Yuan and Wek, Ronald C
The Journal of biological chemistry, ISSN 0021-9258, 04/2005, Volume 280, Issue 14, pp. 14189 - 14202
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Protein Kinases - metabolism | Phosphorylation | Protein Biosynthesis | Protein Kinases - genetics | Ubiquitin - metabolism | Activating Transcription Factor 4 | Protein Subunits - metabolism | Antineoplastic Agents - metabolism | DNA-Binding Proteins - metabolism | RNA Splicing | Transcription Factor CHOP | Trans-Activators - genetics | Eukaryotic Initiation Factor-2 - metabolism | Membrane Proteins - metabolism | CCAAT-Enhancer-Binding Proteins - genetics | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Fibroblasts - metabolism | Protein Subunits - genetics | CCAAT-Enhancer-Binding Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Gene Expression Regulation | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Regulatory Factor X Transcription Factors | Mice, Knockout | Transcription Factors - metabolism | Animals | Eukaryotic Initiation Factor-2 - genetics | Trans-Activators - metabolism | Fibroblasts - cytology | Mice | Apoptosis - physiology | Proteasome Endopeptidase Complex - metabolism | Proteasome Inhibitors | Index Medicus
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2. Full Text Regulation of an eukaryotic initiation factor-2 (eIF-2) associated 67 kDa glycoprotein (p67) and its requirement in protein synthesis
by Gupta, S and Wu Shiyong, Shiyong and Chatterjee, N and Ilan, J and Ilan, J and Osterman, J.C and Gupta, N.K
Gene expression, ISSN 1052-2166, 1995, Volume 5, Issue 2, pp. 113 - 122
Genetics & Heredity | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Glycoproteins - genetics | Transformation, Genetic | Cell Line | Up-Regulation | Phosphorylation | Protein Biosynthesis | Tetradecanoylphorbol Acetate - pharmacology | Aminopeptidases | RNA, Messenger - genetics | Glycoproteins - metabolism | Rats | Immunoblotting | RNA, Messenger - metabolism | DNA, Antisense - genetics | Animals | Eukaryotic Initiation Factor-2 - metabolism | Kinetics | Index Medicus
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3. Full Text DNA immunization with eukaryotic initiation factor-2α of Toxoplasma gondii induces protective immunity against acute and chronic toxoplasmosis in mice
by Chen, Jia and Huang, Si-Yang and Zhou, Dong-Hui and Li, Zhong-Yuan and Petersen, Eskild and Song, Hui-Qun and Zhu, Xing-Quan
Vaccine, ISSN 0264-410X, 2013, Volume 31, Issue 52, pp. 6225 - 6231
Allergy and Immunology | DNA vaccine | Eukaryotic initiation factor-2α (TgIF2α) | Mice | Toxoplasma gondii | Protective immunity | Toxoplasmosis | Immunology | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Fundamental and applied biological sciences. Psychology | Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) | Infectious diseases | Microbiology | Applied microbiology | Parasitic diseases | Protozoal diseases | Biological and medical sciences | Human protozoal diseases | Medical sciences | Toxoplasma - immunology | Vaccines, DNA - genetics | Virulence Factors - genetics | Immunoglobulin G - blood | Vaccines, DNA - immunology | Virulence Factors - immunology | Protozoan Proteins - genetics | Th1 Cells - immunology | Toxoplasmosis, Animal - prevention & control | Vaccines, DNA - administration & dosage | CD4-Positive T-Lymphocytes - immunology | Antibodies, Protozoan - blood | Toxoplasmosis, Animal - parasitology | Female | Brain - parasitology | Disease Models, Animal | Protozoan Vaccines - genetics | Protozoan Vaccines - immunology | Interferon-gamma - secretion | Injections, Intramuscular | Protozoan Vaccines - administration & dosage | Animals | Toxoplasma - genetics | Eukaryotic Initiation Factor-2 - genetics | Survival Analysis | Toxoplasmosis, Animal - immunology | Brain - pathology | CD8-Positive T-Lymphocytes - immunology | Eukaryotic Initiation Factor-2 - immunology | Interleukin-2 - secretion | Protozoan Proteins - immunology | Toxoplasmosis, Animal - pathology | Index Medicus
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4. Full Text eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition
by Simonetti, Angelita and Brito Querido, Jailson and Myasnikov, Alexander G and Mancera-Martinez, Eder and Renaud, Adeline and Kuhn, Lauriane and Hashem, Yaser
Molecular cell, ISSN 1097-2765, 07/2016, Volume 63, Issue 2, pp. 206 - 217
ribosome | eukaryotic translation initiation | eIF3 peripheral subunits | cryo-EM | eIF3 | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Subunits | Protein Biosynthesis | Eukaryotic Initiation Factor-2 - chemistry | Eukaryotic Initiation Factor-3 - chemistry | Humans | Multiprotein Complexes | Ribosomes - metabolism | Structure-Activity Relationship | RNA, Messenger - metabolism | Eukaryotic Initiation Factor-2 - metabolism | Eukaryotic Initiation Factor-1 - chemistry | Eukaryotic Initiation Factor-1 - metabolism | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | Rabbits | RNA, Transfer - metabolism | RNA, Messenger - genetics | Ribosomes - chemistry | Models, Molecular | Eukaryotic Initiation Factor-3 - metabolism | Codon, Initiator | Animals | beta-Globins - metabolism | Protein Binding | Protein Conformation | RNA, Messenger - chemistry | beta-Globins - chemistry | RNA | Genetic translation | Analysis | Index Medicus | Biochemistry, Molecular Biology | Ribosomes | Eukaryotic Initiation Factor-1 | Eukaryotic Initiation Factor-2 | Eukaryotic Initiation Factor-3 | RNA, Transfer | beta-Globins | Life Sciences | Molecular biology | RNA, Messenger
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5. Full Text A Retrospective on eIF2A-and Not the Alpha Subunit of eIF2
by Komar, Anton A and Merrick, William C
International journal of molecular sciences, ISSN 1422-0067, 03/2020, Volume 21, Issue 6, p. 2054
Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Multidisciplinary | Science & Technology | Protein Biosynthesis | Signal Transduction | Eukaryotic Initiation Factor-2 - chemistry | RNA, Transfer - metabolism | Humans | Stress, Physiological | Peptide Chain Initiation, Translational | Structure-Activity Relationship | Mammals | RNA, Messenger - metabolism | Gene Knockdown Techniques | Mice, Knockout | Yeasts - genetics | Animals | Carrier Proteins - metabolism | Eukaryotic Initiation Factor-2 - genetics | Transcription Initiation Site | Eukaryotic Initiation Factor-2 - metabolism | Protein Binding | Prokaryotic Initiation Factor-2 - metabolism | RNA, Messenger - chemistry | Prokaryotic Initiation Factor-2 - chemistry | Evolution, Molecular | Yeasts - metabolism | Binding | Phosphorylation | Polypeptides | Prokaryotes | Translation initiation | Chemical reactions | Homology | Chains | Protein biosynthesis | mRNA | Recruitment | Proteins | Eukaryotes | Protein synthesis | Initiation factor eIF-2 | Binding sites | Structure-function relationships | Transfer RNA | Index Medicus | eif2a | alternative initiation | non-aug initiation | stress response | translational initiation
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6. Full Text Endogenous siRNAs from naturally formed dsRNAs regulate transcripts in mouse oocytes
by Watanabe, Toshiaki and Totoki, Yasushi and Toyoda, Atsushi and Kaneda, Masahiro and Kuramochi-Miyagawa, Satomi and Obata, Yayoi and Chiba, Hatsune and Kohara, Yuji and Kono, Tomohiro and Nakano, Toru and Surani, M. Azim and Sakaki, Yoshiyuki and Sasaki, Hiroyuki
Nature (London), ISSN 0028-0836, 05/2008, Volume 453, Issue 7194, pp. 539 - 543
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Transcription. Transcription factor. Splicing. Rna processing | Molecular and cellular biology | Molecular genetics | RNA, Small Interfering - genetics | Molecular Sequence Data | RNA, Messenger - metabolism | Retroelements - genetics | Eukaryotic Initiation Factor-2 - deficiency | Pseudogenes - genetics | RNA Interference | Gene Expression Regulation, Developmental | Polymerase Chain Reaction | Eukaryotic Initiation Factor-2 - metabolism | Female | RNA, Double-Stranded - metabolism | Oocytes - growth & development | Ribonuclease III - genetics | Ribonuclease III - metabolism | Gene Library | Oocytes - metabolism | Mice, Inbred C57BL | RNA, Messenger - genetics | Ribonuclease III - deficiency | Animals | Eukaryotic Initiation Factor-2 - genetics | RNA, Double-Stranded - genetics | Argonaute Proteins | Mice | RNA, Small Interfering - metabolism | Genetic aspects | RNA | Properties | Oocytes | Life sciences | Ribonucleic acid--RNA | Genes | Rodents | Index Medicus
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7. Full Text Structural and Functional Insights into Human Re-initiation Complexes
by Weisser, Melanie and Schäfer, Tanja and Leibundgut, Marc and Böhringer, Daniel and Aylett, Christopher Herbert Stanley and Ban, Nenad
Molecular cell, ISSN 1097-2765, 08/2017, Volume 67, Issue 3, pp. 447 - 456.e7
eIF2D | ligatin | start codon recognition | translation initiation | DENR | ribosomal recycling | translation regulation | translation re-initiation | MCT-1 | initiator tRNA | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Oncogene Proteins - genetics | Ribosome Subunits, Small, Eukaryotic - chemistry | Eukaryotic Initiation Factor-2 - chemistry | Humans | Multiprotein Complexes | Crystallography, X-Ray | Structure-Activity Relationship | RNA, Messenger - metabolism | Cell Cycle Proteins - chemistry | Transfection | HEK293 Cells | Cell Cycle Proteins - genetics | Eukaryotic Initiation Factor-2 - metabolism | RNA, Transfer - genetics | Transcription Initiation, Genetic | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | Ribosome Subunits, Small, Eukaryotic - genetics | Eukaryotic Initiation Factors - chemistry | Eukaryotic Initiation Factors - genetics | Eukaryotic Initiation Factors - metabolism | Oncogene Proteins - chemistry | RNA, Transfer - metabolism | RNA, Messenger - genetics | Cell Cycle Proteins - metabolism | Oncogene Proteins - metabolism | Cryoelectron Microscopy | Eukaryotic Initiation Factor-2 - genetics | Transcription Initiation Site | Protein Binding | Protein Conformation | RNA, Messenger - chemistry | Molecular Docking Simulation | Mutation | Ribosome Subunits, Small, Eukaryotic - metabolism | RNA | Molecular biology | Binding proteins | Genetic translation | Protein binding | Index Medicus
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8. Full Text Targeting Phosphorylation of Eukaryotic Initiation Factor-2α to Treat Human Disease
by Fullwood, Melissa J and Zhou, Wei and Shenolikar, Shirish
2012, ISBN 0123964563, Volume 106
Neoplasms - metabolism | Guanabenz - therapeutic use | Thiourea - therapeutic use | Humans | Phosphoprotein Phosphatases - metabolism | Eukaryotic Cells - metabolism | Thiourea - pharmacology | Endoplasmic Reticulum Stress - genetics | Molecular Targeted Therapy | Neurodegenerative Diseases - drug therapy | Protein Processing, Post-Translational - drug effects | Protein Folding - drug effects | Eukaryotic Initiation Factor-2 - metabolism | Phosphorylation - drug effects | Unfolded Protein Response - drug effects | Atherosclerosis - drug therapy | Endoplasmic Reticulum Stress - drug effects | Unfolded Protein Response - genetics | Diabetes Mellitus - drug therapy | Diabetes Mellitus - metabolism | Mice, Transgenic | Phosphoprotein Phosphatases - antagonists & inhibitors | Neurodegenerative Diseases - metabolism | Cinnamates - pharmacology | Atherosclerosis - metabolism | Gene Knock-In Techniques | Mice, Knockout | Neoplasms - drug therapy | Guanabenz - pharmacology | Animals | Models, Biological | Protein Biosynthesis - drug effects | Mice | Proteasome Endopeptidase Complex - metabolism | Cinnamates - therapeutic use | Thiourea - analogs & derivatives | Endoplasmic Reticulum Stress - physiology | Index Medicus
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9. Full Text Sustained translational repression by eIF2α-P mediates prion neurodegeneration
by Moreno, Julie A and Radford, Helois and Peretti, Diego and Steinert, Joern R and Verity, Nicholas and Martin, Maria Guerra and Halliday, Mark and Morgan, Jason and Dinsdale, David and Ortori, Catherine A and Barrett, David A and Tsaytler, Pavel and Bertolotti, Anne and Willis, Anne E and Bushell, Martin and Mallucci, Giovanna R
Nature (London), ISSN 0028-0836, 05/2012, Volume 485, Issue 7399, pp. 507 - 511
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Neurology | Organic mental disorders. Neuropsychology | Psychology. Psychoanalysis. Psychiatry | Adult and adolescent clinical studies | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | Psychopathology. Psychiatry | Biological and medical sciences | Medical sciences | Neurons - pathology | Neuroprotective Agents | Phosphorylation | Prions - genetics | Eukaryotic Initiation Factor-2 - chemistry | Neurodegenerative Diseases - etiology | PrPSc Proteins - analysis | Synapses - pathology | Thiourea - pharmacology | Phosphoproteins - metabolism | Repressor Proteins - analysis | PrPSc Proteins - metabolism | Synapses - metabolism | Phosphoproteins - analysis | Protein Folding - drug effects | Protein Phosphatase 1 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Synaptic Transmission - drug effects | Cell Death - drug effects | PrPSc Proteins - toxicity | Neurons - drug effects | Repressor Proteins - metabolism | Prions - metabolism | Synapses - drug effects | Repressor Proteins - chemistry | Neurodegenerative Diseases - pathology | Mice, Inbred C57BL | Kaplan-Meier Estimate | Hippocampus - pathology | Prion Diseases - pathology | Neurodegenerative Diseases - metabolism | Hippocampus - cytology | Cinnamates - pharmacology | Eukaryotic Initiation Factor-2 - analysis | Hippocampus - metabolism | Protein Phosphatase 1 - metabolism | Animals | Prions - biosynthesis | Protein Biosynthesis - drug effects | Mice | Unfolded Protein Response - physiology | Thiourea - analogs & derivatives | Index Medicus
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